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Bone marrow stromal antigen 2 (BST-2) (HM1.24 antigen) (Tetherin) (CD antigen CD317)

 BST2_HUMAN              Reviewed;         180 AA.
Q10589; A8K4Y4; Q53G07;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 152.
RecName: Full=Bone marrow stromal antigen 2;
Short=BST-2;
AltName: Full=HM1.24 antigen;
AltName: Full=Tetherin;
AltName: CD_antigen=CD317;
Flags: Precursor;
Name=BST2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7607676; DOI=10.1016/0888-7543(95)80171-H;
Ishikawa J., Kaisho T., Tomizawa H., Lee B.O., Kobune Y., Inazawa J.,
Oritani K., Itoh M., Ochi T., Ishihara K., Hirano T.;
"Molecular cloning and chromosomal mapping of a bone marrow stromal
cell surface gene, BST2, that may be involved in pre-B-cell growth.";
Genomics 26:527-534(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
SUBUNIT.
PubMed=10329429; DOI=10.1006/bbrc.1999.0683;
Ohtomo T., Sugamata Y., Ozaki Y., Ono K., Yoshimura Y., Kawai S.,
Koishihara Y., Ozaki S., Kosaka M., Hirano T., Tsuchiya M.;
"Molecular cloning and characterization of a surface antigen
preferentially overexpressed on multiple myeloma cells.";
Biochem. Biophys. Res. Commun. 258:583-591(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
TISSUE SPECIFICITY, INDUCTION BY B-CELL ACTIVATION, AND NOMENCLATURE.
PubMed=16157322; DOI=10.1016/j.cellimm.2005.08.002;
Vidal-Laliena M., Romero X., March S., Requena V., Petriz J.,
Engel P.;
"Characterization of antibodies submitted to the B cell section of the
8th Human Leukocyte Differentiation Antigens Workshop by flow
cytometry and immunohistochemistry.";
Cell. Immunol. 236:6-16(2005).
[9]
GPI-ANCHOR [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16602701; DOI=10.1021/pr050419u;
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,
Brodbeck U., Peck S.C., Jensen O.N.;
"Modification-specific proteomics of plasma membrane proteins:
identification and characterization of glycosylphosphatidylinositol-
anchored proteins released upon phospholipase D treatment.";
J. Proteome Res. 5:935-943(2006).
[10]
FUNCTION IN HIV-1 INFECTION.
PubMed=18342597; DOI=10.1016/j.chom.2008.03.001;
Van Damme N., Goff D., Katsura C., Jorgenson R.L., Mitchell R.,
Johnson M.C., Stephens E.B., Guatelli J.;
"The interferon-induced protein BST-2 restricts HIV-1 release and is
downregulated from the cell surface by the viral Vpu protein.";
Cell Host Microbe 3:245-252(2008).
[11]
FUNCTION IN HIV-1 INFECTION.
PubMed=18200009; DOI=10.1038/nature06553;
Neil S.J., Zang T., Bieniasz P.D.;
"Tetherin inhibits retrovirus release and is antagonized by HIV-1
Vpu.";
Nature 451:425-430(2008).
[12]
FUNCTION IN HIV-1 INFECTION, GLYCOSYLATION AT ASN-65 AND ASN-92,
SUBCELLULAR LOCATION, DISULFIDE BONDS, SUBUNIT, TOPOLOGY, GPI-ANCHOR,
AND MUTAGENESIS OF ASN-65 AND ASN-92.
PubMed=19879838; DOI=10.1016/j.cell.2009.08.039;
Perez-Caballero D., Zang T., Ebrahimi A., McNatt M.W., Gregory D.A.,
Johnson M.C., Bieniasz P.D.;
"Tetherin inhibits HIV-1 release by directly tethering virions to
cells.";
Cell 139:499-511(2009).
[13]
REVIEW.
PubMed=19917491; DOI=10.1016/j.chom.2009.11.002;
Gupta R.K., Towers G.J.;
"A tail of Tetherin: how pandemic HIV-1 conquered the world.";
Cell Host Microbe 6:393-395(2009).
[14]
INTERACTION WITH HIV-1 VPU, AND INDUCTION BY HIV-1 VPU.
PubMed=19837671; DOI=10.1074/jbc.M109.058305;
Iwabu Y., Fujita H., Kinomoto M., Kaneko K., Ishizaka Y., Tanaka Y.,
Sata T., Tokunaga K.;
"HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin
through transmembrane interactions leading to lysosomes.";
J. Biol. Chem. 284:35060-35072(2009).
[15]
FUNCTION, AND INTERACTION WITH LILRA4/ILT7.
PubMed=19564354; DOI=10.1084/jem.20090547;
Cao W., Bover L., Cho M., Wen X., Hanabuchi S., Bao M., Rosen D.B.,
Wang Y.H., Shaw J.L., Du Q., Li C., Arai N., Yao Z., Lanier L.L.,
Liu Y.J.;
"Regulation of TLR7/9 responses in plasmacytoid dendritic cells by
BST2 and ILT7 receptor interaction.";
J. Exp. Med. 206:1603-1614(2009).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19036818; DOI=10.1128/JVI.02211-08;
Jouvenet N., Neil S.J., Zhadina M., Zang T., Kratovac Z., Lee Y.,
McNatt M., Hatziioannou T., Bieniasz P.D.;
"Broad-spectrum inhibition of retroviral and filoviral particle
release by tetherin.";
J. Virol. 83:1837-1844(2009).
[18]
INTERACTION WITH HIV-2 ENV, SUBCELLULAR LOCATION, AND INDUCTION BY
HIV-2 ENV.
PubMed=19740980; DOI=10.1128/JVI.01515-09;
Le Tortorec A., Neil S.J.;
"Antagonism to and intracellular sequestration of human tetherin by
the human immunodeficiency virus type 2 envelope glycoprotein.";
J. Virol. 83:11966-11978(2009).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[20]
FUNCTION, INTERACTION WITH EBOLA GP PROTEIN, AND INDUCTION BY EBOLA GP
PROTEIN.
PubMed=19179289; DOI=10.1073/pnas.0811014106;
Kaletsky R.L., Francica J.R., Agrawal-Gamse C., Bates P.;
"Tetherin-mediated restriction of filovirus budding is antagonized by
the Ebola glycoprotein.";
Proc. Natl. Acad. Sci. U.S.A. 106:2886-2891(2009).
[21]
GLYCOSYLATION AT ASN-65 AND ASN-92, SUBUNIT, AND DISULFIDE BONDS.
PubMed=19737401; DOI=10.1186/1742-4690-6-80;
Andrew A.J., Miyagi E., Kao S., Strebel K.;
"The formation of cysteine-linked dimers of BST-2/tetherin is
important for inhibition of HIV-1 virus release but not for
sensitivity to Vpu.";
Retrovirology 6:80-80(2009).
[22]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20686043; DOI=10.1128/JVI.00103-10;
Radoshitzky S.R., Dong L., Chi X., Clester J.C., Retterer C.,
Spurgers K., Kuhn J.H., Sandwick S., Ruthel G., Kota K., Boltz D.,
Warren T., Kranzusch P.J., Whelan S.P., Bavari S.;
"Infectious Lassa virus, but not filoviruses, is restricted by BST-
2/tetherin.";
J. Virol. 84:10569-10580(2010).
[23]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20943977; DOI=10.1128/JVI.01328-10;
Weidner J.M., Jiang D., Pan X.B., Chang J., Block T.M., Guo J.T.;
"Interferon-induced cell membrane proteins, IFITM3 and tetherin,
inhibit vesicular stomatitis virus infection via distinct
mechanisms.";
J. Virol. 84:12646-12657(2010).
[24]
FUNCTION IN KSHV AND HIV-1 INFECTION, SUBCELLULAR LOCATION,
MUTAGENESIS OF LYS-18 AND LYS-21, AND UBIQUITINATION AT LYS-18 BY KSH
VIRUS E3 UBIQUITIN-PROTEIN LIGASE K5.
PubMed=20419159; DOI=10.1371/journal.ppat.1000843;
Pardieu C., Vigan R., Wilson S.J., Calvi A., Zang T., Bieniasz P.,
Kellam P., Towers G.J., Neil S.J.;
"The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1
particle release by mediating ubiquitin-dependent endosomal
degradation of tetherin.";
PLoS Pathog. 6:E1000843-E1000843(2010).
[25]
REVIEW.
PubMed=20688520; DOI=10.1016/j.tim.2010.06.010;
Evans D.T., Serra-Moreno R., Singh R.K., Guatelli J.C.;
"BST-2/tetherin: a new component of the innate immune response to
enveloped viruses.";
Trends Microbiol. 18:388-396(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
REVIEW.
PubMed=22180752; DOI=10.3389/fmicb.2011.00250;
Arias J.F., Iwabu Y., Tokunaga K.;
"structural basis for the antiviral activity of Bst-2/tetherin and its
viral antagonism.";
Front. Microbiol. 2:250-250(2011).
[28]
REVIEW.
PubMed=21166593; DOI=10.1089/jir.2010.0108;
Andrew A., Strebel K.;
"The interferon-inducible host factor bone marrow stromal antigen
2/tetherin restricts virion release, but is it actually a viral
restriction factor?";
J. Interferon Cytokine Res. 31:137-144(2011).
[29]
REVIEW.
PubMed=21222046; DOI=10.1007/s11481-010-9256-1;
Kuhl B.D., Cheng V., Wainberg M.A., Liang C.;
"Tetherin and its viral antagonists.";
J. Neuroimmun. Pharmacol. 6:188-201(2011).
[30]
FUNCTION.
PubMed=21529378; DOI=10.1186/1743-422X-8-198;
Xu F., Tan J., Liu R., Xu D., Li Y., Geng Y., Liang C., Qiao W.;
"Tetherin inhibits prototypic foamy virus release.";
Virol. J. 8:198-198(2011).
[31]
FUNCTION.
PubMed=21621240; DOI=10.1016/j.virol.2011.05.006;
Watanabe R., Leser G.P., Lamb R.A.;
"Influenza virus is not restricted by tetherin whereas influenza VLP
production is restricted by tetherin.";
Virology 417:50-56(2011).
[32]
REVIEW.
PubMed=21994744; DOI=10.3390/v3050520;
Le Tortorec A., Willey S., Neil S.J.;
"Antiviral inhibition of enveloped virus release by tetherin/BST-2:
action and counteraction.";
Viruses 3:520-540(2011).
[33]
REVIEW.
PubMed=22509177; DOI=10.3389/fmicb.2012.00131;
Sato K., Gee P., Koyanagi Y.;
"Vpu and BST2: still not there yet?";
Front. Microbiol. 3:131-131(2012).
[34]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MMP14.
PubMed=22065321; DOI=10.1002/jcb.23433;
Gu G., Zhao D., Yin Z., Liu P.;
"BST-2 binding with cellular MT1-MMP blocks cell growth and migration
via decreasing MMP2 activity.";
J. Cell. Biochem. 113:1013-1021(2012).
[35]
REVIEW.
PubMed=22811908; DOI=10.1155/2012/424768;
Hammonds J., Wang J.J., Spearman P.;
"Restriction of retroviral replication by tetherin/BST-2.";
Mol. Biol. Int. 2012:424768-424768(2012).
[36]
FUNCTION, SUBUNIT, ALTERNATIVE INITIATION (ISOFORMS 1 AND 2),
INDUCTION, AND MUTAGENESIS OF 3-SER--SER-5; TYR-6 AND TYR-8.
PubMed=23028328; DOI=10.1371/journal.ppat.1002931;
Cocka L.J., Bates P.;
"Identification of alternatively translated Tetherin isoforms with
differing antiviral and signaling activities.";
PLoS Pathog. 8:E1002931-E1002931(2012).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[38]
FUNCTION.
PubMed=22520941; DOI=10.1016/j.virol.2012.03.011;
Dafa-Berger A., Kuzmina A., Fassler M., Yitzhak-Asraf H.,
Shemer-Avni Y., Taube R.;
"Modulation of hepatitis C virus release by the interferon-induced
protein BST-2/tetherin.";
Virology 428:98-111(2012).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[40]
X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 87-147, FUNCTION, DOMAIN,
DISULFIDE BONDS, SUBUNIT, SUBCELLULAR LOCATION, AND CIRCULAR
DICHROISM.
PubMed=20399176; DOI=10.1016/j.chom.2010.03.005;
Hinz A., Miguet N., Natrajan G., Usami Y., Yamanaka H., Renesto P.,
Hartlieb B., McCarthy A.A., Simorre J.P., Gottlinger H.,
Weissenhorn W.;
"Structural basis of HIV-1 tethering to membranes by the BST-
2/tetherin ectodomain.";
Cell Host Microbe 7:314-323(2010).
[41]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 47-152, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=20880831; DOI=10.1073/pnas.1008206107;
Schubert H.L., Zhai Q., Sandrin V., Eckert D.M., Garcia-Maya M.,
Saul L., Sundquist W.I., Steiner R.A., Hill C.P.;
"Structural and functional studies on the extracellular domain of
BST2/tetherin in reduced and oxidized conformations.";
Proc. Natl. Acad. Sci. U.S.A. 107:17951-17956(2010).
[42]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 47-161, SUBUNIT, FUNCTION,
AND DISULFIDE BONDS.
PubMed=20940320; DOI=10.1073/pnas.1011485107;
Yang H., Wang J., Jia X., McNatt M.W., Zang T., Pan B., Meng W.,
Wang H.W., Bieniasz P.D., Xiong Y.;
"Structural insight into the mechanisms of enveloped virus tethering
by tetherin.";
Proc. Natl. Acad. Sci. U.S.A. 107:18428-18432(2010).
-!- FUNCTION: IFN-induced antiviral host restriction factor which
efficiently blocks the release of diverse mammalian enveloped
viruses by directly tethering nascent virions to the membranes of
infected cells. Acts as a direct physical tether, holding virions
to the cell membrane and linking virions to each other. The
tethered virions can be internalized by endocytosis and
subsequently degraded or they can remain on the cell surface. In
either case, their spread as cell-free virions is restricted. Its
target viruses belong to diverse families, including retroviridae:
human immunodeficiency virus type 1 (HIV-1), human
immunodeficiency virus type 2 (HIV-2), simian immunodeficiency
viruses (SIVs), equine infectious anemia virus (EIAV), feline
immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason-
Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1
(HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus
(MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola
virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus
(LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma-
associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis
virus (VSV), orthomyxoviridae: influenza A virus, and
paramyxoviridae: nipah virus. Can inhibit cell surface proteolytic
activity of MMP14 causing decreased activation of MMP15 which
results in inhibition of cell growth and migration. Can stimulate
signaling by LILRA4/ILT7 and consequently provide negative
feedback to the production of IFN by plasmacytoid dendritic cells
in response to viral infection. Plays a role in the organization
of the subapical actin cytoskeleton in polarized epithelial cells.
Isoform 1 and isoform 2 are both effective viral restriction
factors but have differing antiviral and signaling activities.
Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and
restricts HIV-1 viral budding in the presence of Vpu. Isoform 1
acts as an activator of NF-kappa-B and this activity is inhibited
by isoform 2. {ECO:0000269|PubMed:18200009,
ECO:0000269|PubMed:18342597, ECO:0000269|PubMed:19036818,
ECO:0000269|PubMed:19179289, ECO:0000269|PubMed:19564354,
ECO:0000269|PubMed:19879838, ECO:0000269|PubMed:20399176,
ECO:0000269|PubMed:20419159, ECO:0000269|PubMed:20686043,
ECO:0000269|PubMed:20940320, ECO:0000269|PubMed:20943977,
ECO:0000269|PubMed:21529378, ECO:0000269|PubMed:21621240,
ECO:0000269|PubMed:22065321, ECO:0000269|PubMed:22520941,
ECO:0000269|PubMed:23028328}.
-!- SUBUNIT: Parallel homodimer; disulfide-linked. May form
homotetramers under reducing conditions. Isoform 1 and isoform 2
form homodimers and also heterodimers with each other.
Dimerization is essential for its antiviral activity. Interacts
(via cytoplasmic domain) with ARHGAP44 (By similarity). Interacts
with MMP14 (via C-terminal cytoplasmic tail). Interacts with
LILRA4/ILT7. Interacts (via transmembrane domain) with HIV-1 VPU
(via transmembrane domain). Interacts with HIV-2 ENV and ebola GP
protein. {ECO:0000250, ECO:0000269|PubMed:10329429,
ECO:0000269|PubMed:19179289, ECO:0000269|PubMed:19564354,
ECO:0000269|PubMed:19737401, ECO:0000269|PubMed:19740980,
ECO:0000269|PubMed:19837671, ECO:0000269|PubMed:19879838,
ECO:0000269|PubMed:20399176, ECO:0000269|PubMed:20880831,
ECO:0000269|PubMed:20940320, ECO:0000269|PubMed:22065321,
ECO:0000269|PubMed:23028328}.
-!- INTERACTION:
P35585:Ap1m1 (xeno); NbExp=2; IntAct=EBI-2476339, EBI-1040251;
P59901:LILRA4; NbExp=2; IntAct=EBI-2476339, EBI-2841591;
P69699:vpu (xeno); NbExp=7; IntAct=EBI-2476339, EBI-10757638;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Cell
membrane; Single-pass type II membrane protein. Cell membrane;
Lipid-anchor, GPI-anchor. Late endosome. Membrane raft. Cytoplasm.
Apical cell membrane {ECO:0000250}. Note=Shuttles between the cell
membrane, where it is present predominantly in membrane/lipid
rafts, and the trans-Golgi network. HIV-1 VPU and HIV-2 ENV can
target it to the trans-Golgi network thus sequestering it away
from virus assembly sites on the cell membrane. Targeted to late
endosomes upon KSHV infection and subsequent ubiquitination. Forms
a complex with MMP14 and localizes to the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1; Synonyms=l-Tetherin;
IsoId=Q10589-1; Sequence=Displayed;
Name=2; Synonyms=s-Tetherin;
IsoId=Q10589-2; Sequence=VSP_053250;
Note=Produced by alternative initiation at Met-13 of isoform 1.;
-!- TISSUE SPECIFICITY: Predominantly expressed in liver, lung, heart
and placenta. Lower levels in pancreas, kidney, skeletal muscle
and brain. Overexpressed in multiple myeloma cells. Highly
expressed during B-cell development, from pro-B precursors to
plasma cells. Highly expressed on T-cells, monocytes, NK cells and
dendritic cells (at protein level). {ECO:0000269|PubMed:10329429,
ECO:0000269|PubMed:16157322}.
-!- INDUCTION: By type I interferons. Down-regulated by viral
antagonistic factors which include: HIV-1 VPU protein, HIV-2 ENV
protein, KSHV K5 protein and ebola virus GP protein. VPU and ENV
antagonize its function by targeting it to the trans-Golgi
network, sequestering it away from virus assembly sites on the
cell membrane. VPU also acts as an adapter molecule linking it to
BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box
protein E3 ubiquitin ligase, inducing its ubiquitination and
subsequent proteasomal degradation. K5 ubiquitinates it leading to
its targeting to late endosomes and degradation.
{ECO:0000269|PubMed:16157322, ECO:0000269|PubMed:19179289,
ECO:0000269|PubMed:19740980, ECO:0000269|PubMed:19837671,
ECO:0000269|PubMed:23028328}.
-!- DOMAIN: The extracellular coiled coil domain forms an extended 170
A long semi-flexible rod-like structure important for virion
retention at the cell surface and prevention of virus spreading.
{ECO:0000269|PubMed:20399176}.
-!- PTM: Monoubiquitinated by KSHV E3 ubiquitin-protein ligase K5,
leading to its targeting to late endosomes and degradation.
{ECO:0000269|PubMed:20419159}.
-!- PTM: The GPI anchor is essential for its antiviral activity.
-!- MISCELLANEOUS: Tetherin shows evidence of positive (adaptive)
selection, presumably as a result of evolutionary pressure applied
by antagonistic viral proteins that counteract its inhibitiory
activity and this has led to the species-specific tetherin
sensitivity to viral countermeasures. For example, Tantalus monkey
tetherin cannot be abrogated by HIV-1 VPU due to variation in the
tetherin transmembrane region. Similarly, SIV Nefs are able to
overcome simian tetherins, but not human tetherin, due to a unique
5-amino-acid deletion in the cytoplasmic tail domain of human
tetherin (PubMed:19917491). {ECO:0000305|PubMed:19917491}.
-!- SIMILARITY: Belongs to the tetherin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D28137; BAA05679.1; -; mRNA.
EMBL; AK223124; BAD96844.1; -; mRNA.
EMBL; AK291099; BAF83788.1; -; mRNA.
EMBL; AC010319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84602.1; -; Genomic_DNA.
EMBL; BC033873; AAH33873.1; -; mRNA.
CCDS; CCDS12358.1; -. [Q10589-1]
PIR; A56836; A56836.
RefSeq; NP_004326.1; NM_004335.3. [Q10589-1]
UniGene; Hs.118110; -.
PDB; 2LK9; NMR; -; A=18-47.
PDB; 2X7A; X-ray; 2.77 A; A/B/C/D/E/F/G/H/I/J/K=87-147.
PDB; 2XG7; X-ray; 3.45 A; A/C=51-151.
PDB; 3MQ7; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I/J/K/L=47-161.
PDB; 3MQ9; X-ray; 2.80 A; A/B/C/D/E/F/G/H=66-139.
PDB; 3MQB; X-ray; 3.20 A; A/B/E/F=47-161.
PDB; 3MQC; X-ray; 2.80 A; A/B/C/D=47-161.
PDB; 3NWH; X-ray; 2.60 A; A/B/C/D=47-152.
PDB; 4P6Z; X-ray; 3.00 A; T=1-21.
PDBsum; 2LK9; -.
PDBsum; 2X7A; -.
PDBsum; 2XG7; -.
PDBsum; 3MQ7; -.
PDBsum; 3MQ9; -.
PDBsum; 3MQB; -.
PDBsum; 3MQC; -.
PDBsum; 3NWH; -.
PDBsum; 4P6Z; -.
ProteinModelPortal; Q10589; -.
SMR; Q10589; -.
BioGrid; 107149; 16.
DIP; DIP-53216N; -.
IntAct; Q10589; 15.
MINT; MINT-8402291; -.
STRING; 9606.ENSP00000252593; -.
iPTMnet; Q10589; -.
PhosphoSitePlus; Q10589; -.
SwissPalm; Q10589; -.
DMDM; 1705508; -.
EPD; Q10589; -.
MaxQB; Q10589; -.
PaxDb; Q10589; -.
PeptideAtlas; Q10589; -.
PRIDE; Q10589; -.
DNASU; 684; -.
Ensembl; ENST00000252593; ENSP00000252593; ENSG00000130303. [Q10589-1]
GeneID; 684; -.
KEGG; hsa:684; -.
UCSC; uc060vid.1; human. [Q10589-1]
CTD; 684; -.
DisGeNET; 684; -.
EuPathDB; HostDB:ENSG00000130303.12; -.
GeneCards; BST2; -.
HGNC; HGNC:1119; BST2.
HPA; HPA017060; -.
MIM; 600534; gene.
neXtProt; NX_Q10589; -.
OpenTargets; ENSG00000130303; -.
PharmGKB; PA25436; -.
eggNOG; ENOG410JE1U; Eukaryota.
eggNOG; ENOG41115GP; LUCA.
GeneTree; ENSGT00390000013782; -.
HOGENOM; HOG000013084; -.
HOVERGEN; HBG004902; -.
InParanoid; Q10589; -.
KO; K06731; -.
OMA; LNHKLQD; -.
OrthoDB; EOG091G1B7U; -.
PhylomeDB; Q10589; -.
TreeFam; TF338345; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
ChiTaRS; BST2; human.
EvolutionaryTrace; Q10589; -.
GeneWiki; Tetherin; -.
GenomeRNAi; 684; -.
PRO; PR:Q10589; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130303; -.
CleanEx; HS_BST2; -.
ExpressionAtlas; Q10589; baseline and differential.
Genevisible; Q10589; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0009986; C:cell surface; IMP:CACAO.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005771; C:multivesicular body; IMP:CACAO.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:1901253; P:negative regulation of intracellular transport of viral material; IDA:UniProtKB.
GO; GO:0002737; P:negative regulation of plasmacytoid dendritic cell cytokine production; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0035455; P:response to interferon-alpha; ISS:UniProtKB.
GO; GO:0035456; P:response to interferon-beta; ISS:UniProtKB.
GO; GO:0034341; P:response to interferon-gamma; ISS:UniProtKB.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
InterPro; IPR024886; BST2.
PANTHER; PTHR15190; PTHR15190; 1.
Pfam; PF16716; BST2; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Antiviral defense;
B-cell activation; Cell membrane; Coiled coil; Complete proteome;
Cytoplasm; Disulfide bond; Endosome; Glycoprotein; Golgi apparatus;
GPI-anchor; Immunity; Innate immunity; Isopeptide bond; Lipoprotein;
Membrane; Polymorphism; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 161 Bone marrow stromal antigen 2.
/FTId=PRO_0000065005.
PROPEP 162 180 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000253552.
TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.
TRANSMEM 21 48 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 49 161 Extracellular. {ECO:0000255}.
COILED 68 152
LIPID 161 161 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19737401,
ECO:0000269|PubMed:19879838}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19737401,
ECO:0000269|PubMed:19879838}.
DISULFID 53 53 Interchain.
DISULFID 63 63 Interchain.
DISULFID 91 91 Interchain.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20419159}.
VAR_SEQ 1 12 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053250.
VARIANT 143 143 V -> F (in dbSNP:rs1804402).
/FTId=VAR_012067.
MUTAGEN 3 5 STS->AAA: Partial resistance to Vpu.
{ECO:0000269|PubMed:23028328}.
MUTAGEN 6 6 Y->A: Partial resistance to Vpu and
significantly reduced activation of NF-
kB; when associated with A-8.
{ECO:0000269|PubMed:23028328}.
MUTAGEN 8 8 Y->A: Partial resistance to Vpu and
significantly reduced activation of NF-
kB; when associated with A-6.
{ECO:0000269|PubMed:23028328}.
MUTAGEN 18 18 K->R: Abolishes redistribution to late
endosomes in cells expressing KSH virus
E3 ubiquitin-protein ligase K5.
{ECO:0000269|PubMed:20419159}.
MUTAGEN 21 21 K->R: No effect on redistribution to late
endosomes in cells expressing KSH virus
E3 ubiquitin-protein ligase K5.
{ECO:0000269|PubMed:20419159}.
MUTAGEN 65 65 N->A: Loss of glycosylation site.
{ECO:0000269|PubMed:19879838}.
MUTAGEN 92 92 N->A: Loss of glycosylation site. Impairs
anti-viral activity.
{ECO:0000269|PubMed:19879838}.
CONFLICT 141 141 N -> D (in Ref. 4; BAD96844).
{ECO:0000305}.
HELIX 23 44 {ECO:0000244|PDB:2LK9}.
HELIX 52 148 {ECO:0000244|PDB:3MQ7}.
STRAND 152 154 {ECO:0000244|PDB:3MQB}.
SEQUENCE 180 AA; 19769 MW; CAF52340D69061EE CRC64;
MASTSYDYCR VPMEDGDKRC KLLLGIGILV LLIIVILGVP LIIFTIKANS EACRDGLRAV
MECRNVTHLL QQELTEAQKG FQDVEAQAAT CNHTVMALMA SLDAEKAQGQ KKVEELEGEI
TTLNHKLQDA SAEVERLRRE NQVLSVRIAD KKYYPSSQDS SSAAAPQLLI VLLGLSALLQ


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